ID   MHPC1_PSEPU             Reviewed;         285 AA.
AC   Q49KF8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_01654};
DE            EC=3.7.1.14 {ECO:0000255|HAMAP-Rule:MF_01654};
DE   AltName: Full=2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_01654};
DE   AltName: Full=2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_01654};
DE   AltName: Full=2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_01654};
GN   Name=mhpC1 {ECO:0000255|HAMAP-Rule:MF_01654}; Synonyms=cbzF;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid pKW1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GJ31;
RA   Reineke W., Kunze M.;
RT   "GJ31 meta-operon.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6-
CC       oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol ring
CC       fission product of the bacterial meta-cleavage pathway for degradation
CC       of phenylpropionic acid. {ECO:0000255|HAMAP-Rule:MF_01654}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,4E)-2-hydroxy-6-oxonona-2,4-dienedioate + H2O = (2Z)-2-
CC         hydroxypenta-2,4-dienoate + H(+) + succinate; Xref=Rhea:RHEA:34187,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:66887, ChEBI:CHEBI:67152; EC=3.7.1.14;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01654};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-trienedioate + H2O =
CC         (2Z)-2-hydroxypenta-2,4-dienoate + fumarate + H(+);
CC         Xref=Rhea:RHEA:34191, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29806, ChEBI:CHEBI:66888, ChEBI:CHEBI:67152; EC=3.7.1.14;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01654};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_01654}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01654}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MhpC family.
CC       {ECO:0000255|HAMAP-Rule:MF_01654}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX50133.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY831461; AAX50133.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q49KF8; -.
DR   SMR; Q49KF8; -.
DR   ESTHER; psepu-mhpc1; Carbon-carbon_bond_hydrolase.
DR   UniPathway; UPA00714; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0052823; F:2-hydroxy-6-oxonona-2,4,7-trienedioate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018771; F:2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01654; MhpC; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR023791; MhpC_alpha/beta_hydrolase.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Hydrolase; Plasmid.
FT   CHAIN           1..285
FT                   /note="2-hydroxy-6-oxononadienedioate/2-hydroxy-6-
FT                   oxononatrienedioate hydrolase 1"
FT                   /id="PRO_0000337784"
FT   ACT_SITE        265
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT   SITE            112
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT   SITE            190
FT                   /note="Catalytic role in ketonization of the dienol
FT                   substrate (substrate destabilization)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
SQ   SEQUENCE   285 AA;  31600 MW;  500D187CF7EC9357 CRC64;
     MTAITEKETS KFVRIQDGDL DLNIHYNDCG EGKETVVMLH GSGPGASGWA NFNRNIEPLV
     NAGFRVILMD CPGWSKSDSI VSTGSRSDLN ARVLKGLVDK LDLDKIHILG NSMGGHTAVA
     FSLTWPERVG KLVLMGGGTG GVSPFVPMPS EGIKLLNGLY REPTIENLKK MMSIFVYDTS
     DLTEELFQTR LDNMLARKDH LENFTASLAA NLKQFPDFGH RLGEINAETL VIWGRNDRFV
     PLDTGLRLVA GISNSQLHVF NKCGHWAQWE HADTFNRMVL DFLTH